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1ha7

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(New page: 200px<br /><applet load="1ha7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ha7, resolution 2.20&Aring;" /> '''STRUCTURE OF A LIGHT...)
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[[Image:1ha7.gif|left|200px]]<br /><applet load="1ha7" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ha7.gif|left|200px]]<br /><applet load="1ha7" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ha7, resolution 2.20&Aring;" />
caption="1ha7, resolution 2.20&Aring;" />
'''STRUCTURE OF A LIGHT-HARVESTING PHYCOBILIPROTEIN, C-PHYCOCYANIN FROM SPIRULINA PLATENSIS AT 2.2A RESOLUTION'''<br />
'''STRUCTURE OF A LIGHT-HARVESTING PHYCOBILIPROTEIN, C-PHYCOCYANIN FROM SPIRULINA PLATENSIS AT 2.2A RESOLUTION'''<br />
==Overview==
==Overview==
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The crystal structure of C-phycocyanin, a light-harvesting, phycobiliprotein from cyanobacteria (blue-green algae) Spirulina platensis, has been solved by molecular replacement technique. The crystals belong to, space group P2(1) with cell parameters a = 107.20, b = 115.40, c = 183.04, A; beta = 90.2 degrees. The structure has been refined to a, crystallographic R factor of 19.2% (R(free) = 23.9%) using the X-ray, diffraction data extending up to 2.2 A resolution. The asymmetric unit of, the crystal cell consists of two (alphabeta)6-hexamers, each hexamer being, the functional unit in the native antenna rod of cyanobacteria. The, molecular structure resembles that of other reported C-phycocyanins., However, the unique form of aggregation of two (alphabeta)6-hexamers in, the crystal asymmetric unit, suggests additional pathways of energy, transfer in lateral direction between the adjacent hexamers involving, beta155 phycocyanobilin chromophores.
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The crystal structure of C-phycocyanin, a light-harvesting phycobiliprotein from cyanobacteria (blue-green algae) Spirulina platensis has been solved by molecular replacement technique. The crystals belong to space group P2(1) with cell parameters a = 107.20, b = 115.40, c = 183.04 A; beta = 90.2 degrees. The structure has been refined to a crystallographic R factor of 19.2% (R(free) = 23.9%) using the X-ray diffraction data extending up to 2.2 A resolution. The asymmetric unit of the crystal cell consists of two (alphabeta)6-hexamers, each hexamer being the functional unit in the native antenna rod of cyanobacteria. The molecular structure resembles that of other reported C-phycocyanins. However, the unique form of aggregation of two (alphabeta)6-hexamers in the crystal asymmetric unit, suggests additional pathways of energy transfer in lateral direction between the adjacent hexamers involving beta155 phycocyanobilin chromophores.
==About this Structure==
==About this Structure==
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1HA7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis] with CYC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HA7 OCA].
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1HA7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis] with <scene name='pdbligand=CYC:'>CYC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HA7 OCA].
==Reference==
==Reference==
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[[Category: Arthrospira platensis]]
[[Category: Arthrospira platensis]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Padyana, A.K.]]
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[[Category: Padyana, A K.]]
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[[Category: Rajashankar, K.R.]]
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[[Category: Rajashankar, K R.]]
[[Category: Ramakumar, S.]]
[[Category: Ramakumar, S.]]
[[Category: CYC]]
[[Category: CYC]]
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[[Category: pigment protein]]
[[Category: pigment protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:28:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:59:08 2008''

Revision as of 10:59, 21 February 2008


1ha7, resolution 2.20Å

Drag the structure with the mouse to rotate

STRUCTURE OF A LIGHT-HARVESTING PHYCOBILIPROTEIN, C-PHYCOCYANIN FROM SPIRULINA PLATENSIS AT 2.2A RESOLUTION

Overview

The crystal structure of C-phycocyanin, a light-harvesting phycobiliprotein from cyanobacteria (blue-green algae) Spirulina platensis has been solved by molecular replacement technique. The crystals belong to space group P2(1) with cell parameters a = 107.20, b = 115.40, c = 183.04 A; beta = 90.2 degrees. The structure has been refined to a crystallographic R factor of 19.2% (R(free) = 23.9%) using the X-ray diffraction data extending up to 2.2 A resolution. The asymmetric unit of the crystal cell consists of two (alphabeta)6-hexamers, each hexamer being the functional unit in the native antenna rod of cyanobacteria. The molecular structure resembles that of other reported C-phycocyanins. However, the unique form of aggregation of two (alphabeta)6-hexamers in the crystal asymmetric unit, suggests additional pathways of energy transfer in lateral direction between the adjacent hexamers involving beta155 phycocyanobilin chromophores.

About this Structure

1HA7 is a Protein complex structure of sequences from Arthrospira platensis with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of a light-harvesting protein C-phycocyanin from Spirulina platensis., Padyana AK, Bhat VB, Madyastha KM, Rajashankar KR, Ramakumar S, Biochem Biophys Res Commun. 2001 Apr 13;282(4):893-8. PMID:11352634

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